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Mannanase hydrolysis of spruce galactoglucomannan focusing on the influence of acetylation on enzymatic mannan degradation
Chalmers Univ Technol, Div Ind Biotechnol, Dept Biol & Biol Engn, S-41296 Gothenburg, Sweden.;Chalmers Univ Technol, Wallenberg Wood Sci Ctr, S-41296 Gothenburg, Sweden..
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry, Glycoscience.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Centres, Wallenberg Wood Science Center.
Chalmers Univ Technol, Div Ind Biotechnol, Dept Biol & Biol Engn, S-41296 Gothenburg, Sweden.;Chalmers Univ Technol, Wallenberg Wood Sci Ctr, S-41296 Gothenburg, Sweden..
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2018 (English)In: Biotechnology for Biofuels, ISSN 1754-6834, E-ISSN 1754-6834, Vol. 11, article id 114Article in journal (Refereed) Published
Abstract [en]

Background: Galactoglucomannan (GGM) is the most abundant hemicellulose in softwood, and consists of a backbone of mannose and glucose units, decorated with galactose and acetyl moieties. GGM can be hydrolyzed into fermentable sugars, or used as a polymer in films, gels, and food additives. Endo-beta-mannanases, which can be found in the glycoside hydrolase families 5 and 26, specifically cleave the mannan backbone of GGM into shorter oligosaccharides. Information on the activity and specificity of different mannanases on complex and acetylated substrates is still lacking. The aim of this work was to evaluate and compare the modes of action of two mannanases from Cellvibrio japonicus (CjMan5A and CjMan26A) on a variety of mannan substrates, naturally and chemically acetylated to varying degrees, including naturally acetylated spruce GGM. Both enzymes were evaluated in terms of cleavage patterns and their ability to accommodate acetyl substitutions. Results: CjMan5A and CjMan26A demonstrated different substrate preferences on mannan substrates with distinct backbone and decoration structures. CjMan5A action resulted in higher amounts of mannotriose and mannotetraose than that of CjMan26A, which mainly generated mannose and mannobiose as end products. Mass spectrometric analysis of products from the enzymatic hydrolysis of spruce GGM revealed that an acetylated hexotriose was the shortest acetylated oligosaccharide produced by CjMan5A, whereas CjMan26A generated acetylated hexobiose as well as diacetylated oligosaccharides. A low degree of native acetylation did not significantly inhibit the enzymatic action. However, a high degree of chemical acetylation resulted in decreased hydrolyzability of mannan substrates, where reduced substrate solubility seemed to reduce enzyme activity. Conclusions: Our findings demonstrate that the two mannanases from C. japonicus have different cleavage patterns on linear and decorated mannan polysaccharides, including the abundant and industrially important resource spruce GGM. CjMan26A released higher amounts of fermentable sugars suitable for biofuel production, while CjMan5A, producing higher amounts of oligosaccharides, could be a good candidate for the production of oligomeric platform chemicals and food additives. Furthermore, chemical acetylation of mannan polymers was found to be a potential strategy for limiting the biodegradation of mannan-containing materials.

Place, publisher, year, edition, pages
BIOMED CENTRAL LTD , 2018. Vol. 11, article id 114
Keywords [en]
Lignocellulose, Spruce, Galactoglucomannan, Endo-beta-mannanases, GH5, GH26, Cellvibrio japonicus, Polysaccharide acetylation, Enzymatic degradation pattern, Acetyl esterases
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:kth:diva-227774DOI: 10.1186/s13068-018-1115-yISI: 000430977200001PubMedID: 29713374Scopus ID: 2-s2.0-85045688074OAI: oai:DiVA.org:kth-227774DiVA, id: diva2:1205443
Funder
Knut and Alice Wallenberg FoundationSwedish Research Council, 621-2014-5295
Note

QC 20180514

Available from: 2018-05-14 Created: 2018-05-14 Last updated: 2018-05-14Bibliographically approved

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Martinez-Abad, AntonioBerglund, JennieVilaplana, Francisco
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